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Database: UniProt
Entry: J0S9T1_HELPX
LinkDB: J0S9T1_HELPX
Original site: J0S9T1_HELPX 
ID   J0S9T1_HELPX            Unreviewed;       167 AA.
AC   J0S9T1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=HPHPP15B_1112 {ECO:0000313|EMBL:EJC32278.1};
OS   Helicobacter pylori Hp P-15b.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992108 {ECO:0000313|EMBL:EJC32278.1, ECO:0000313|Proteomes:UP000004543};
RN   [1] {ECO:0000313|EMBL:EJC32278.1, ECO:0000313|Proteomes:UP000004543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp P-15b {ECO:0000313|EMBL:EJC32278.1,
RC   ECO:0000313|Proteomes:UP000004543};
RA   Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA   Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT   "Genome sequence of Helicobacter pylori Hp P-15b.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJC32278.1}.
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DR   EMBL; AKQJ01000003; EJC32278.1; -; Genomic_DNA.
DR   AlphaFoldDB; J0S9T1; -.
DR   PATRIC; fig|992108.3.peg.1072; -.
DR   Proteomes; UP000004543; Unassembled WGS sequence.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EJC32278.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJC32278.1}.
SQ   SEQUENCE   167 AA;  19089 MW;  5F2C2D6D77999A66 CRC64;
     MHANLFNQNA SKKDIFLHNL RSNNGRYKRY VKAPLRYGGG KSLAVGLIVE YIPNGVRRMI
     SPFIGGGSVE IACAAELGLE VLGFDIFDIL VNFYQVLLKD KQALYNHLLS LEPTQETYNI
     IKQELKAHYK KECVLDPLIL ARDYYFNFNL SYGPGFLGWM SKIYTEK
//
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